The enzymatic synthesis of poly 4-thiouridylic acid by polynucleotide phosphorylase from Escherichia coli

Add time:09/09/2019    Source:sciencedirect.com

4-Thiouridine 5′-diphosphate (s4UDP) was found to be a substrate for polynucleotide phosphorylase from Escherichia coli. s4UDP gave β-phosphate exchange (Km = 0.26 mM; vmax = 0.18 μmole/ml per 20 min) and was polymerised to poly 4-thiouridylic acid (poly s4U) (Km = 0.17 mM; vmax = 1.5 mμmoles/0.1 ml per 15 min). In the presence of phosphate poly s4U was degraded by polynucleotide phosphorylase to s4UDP. Poly s4U was isolated on a preparative scale and characterized by means of sedimentation velocity analysis in an ultracentrifuge. Spectral properties of s4U and complex formation of poly s4U with poly A were investigated.

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